9002-07-7 Usage
Description
Trypsin is a serine protease enzyme found in the digestive systems of humans and animals, primarily secreted by the pancreas in an inactive form called trypsinogen. It plays a crucial role in the digestion of proteins by hydrolyzing them into smaller peptides or amino acids. Trypsin is also used in various applications across different industries due to its proteolytic properties.
Uses
Used in Digestive System:
Trypsin is used as a digestive enzyme for breaking down proteins into smaller peptides in the small intestine, aiding in the digestion process.
Used in Tissue Culture:
Trypsin is used as a cell-dissociating agent for releasing adherent cells from tissue culture plates, facilitating passaging and cell growth.
Used in Food Processing Industry:
Trypsin is used as a food processing aid to improve functional properties of food proteins, such as solubility, emulsification, foaming, and gelling. It also helps in reducing allergen concentration, producing protein hydrolysates, and bioactive peptides for infant formulas and people with special health needs.
Used in Food Science Research:
Trypsin is used for food protein sequencing and in-vitro determination of food protein digestibility.
Used in Pharmaceutical Industry:
In combination with bromelain and rutin, trypsin is used for treating osteoarthritis.
Used in Wound and Ulcer Cleaning:
Trypsin is used to remove necrotic tissue and debris during wound and ulcer cleaning, promoting healing.
Used in Surgical Procedures:
Trypsin supplements may be used to remove dead tissue cells remaining after trauma, infection, or surgical procedures, allowing new skin or tissue cells to grow.
Chemical Properties:
Trypsin is a white or almost white, crystalline or amorphous powder that is hygroscopic if amorphous.
Brand Names:
Parenzyme, Trypsillin.
References
[1] http://www.cytospring.com/pages/TrypsinEDTA.pdf
[2] Jianmei Yu, Mohamed Ahmedna (2012) Functions/applications of trypsin in food processing and food science research, 75-95
[3] http://www.webmd.com/vitamins-supplements/ingredientmono-879-trypsin.aspx?activeingredientid=879&activeingredientname=trypsin
Biochem/physiol Actions
Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity. Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Check Digit Verification of cas no
The CAS Registry Mumber 9002-07-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,0 and 2 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 9002-07:
(6*9)+(5*0)+(4*0)+(3*2)+(2*0)+(1*7)=67
67 % 10 = 7
So 9002-07-7 is a valid CAS Registry Number.
